Phagocytosis of yeast: A method for concurrent quantification of binding and internalization using differential interference contrast microscopy

Journal of Immunological Methods

Volumn 238, Issue 1-2, 2000, Pages 29-43

  Bos, Hendrik ^a   De Souza, Wanderley ^a,b  

^a Ctro Biociencias Biotecnologia U   (Brazil)

^b FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

Author keywords

Cytochalasin D; Phagocytosis; Trypan blue

Indexed keywords

CYTOCHALASIN D; HORSERADISH PEROXIDASE;

ANIMAL CELL; ARTICLE; CELL ADHESION; CELL SURFACE; CONTROLLED STUDY; IN VITRO STUDY; INTERNALIZATION; MACROPHAGE; MOUSE; NONHUMAN; PHAGOCYTOSIS; PHASE CONTRAST MICROSCOPY; PRIORITY JOURNAL; TECHNIQUE; YEAST;

ANIMALS; CYTOCHALASIN D; HORSERADISH PEROXIDASE; LIGANDS; MACROPHAGES, PERITONEAL; MICE; MICROSCOPY, INTERFERENCE; MICROSCOPY, PHASE-CONTRAST; PHAGOCYTOSIS; RECEPTORS, IMMUNOLOGIC; SACCHAROMYCES CEREVISIAE;

ARMORACIA RUSTICANA;

EID: 0034697386     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-1759(00)00132-0     Document Type: Article

References (41)

1. Axline S.G., Reaven E.P. Inhibition of phagocytosis and plasma membrane mobility of the cultivated macrophage by cytochalasin B. J. Cell Biol. 62:1974;647.
2. Bacon J.S.D., Farmer V.C., Jones D., Tayler I.F. The glucan components of the cell wall of bakers' yeast (Saccharomyces cerevisiae) considered in relation to its ultrastructure. Biochem. J. 114:1969;557.
3. Blackwell J.M., Ezekowitz R.A.B., Roberts M.B., Channon J.Y., Sim R.B., Gordon S. Macrophage complement and lectin-like receptors bind Leishmania in the absence of serum. J. Exp. Med. 162:1985;324.
4. Boyes E.A., Old L.J., Charoulikov J. Cytotoxity test for demonstration of antibodies. Meth. Med. Res. 10:1964;39.
5. Cooper J.A. Effects of cytochalasin and phalloindin on action. J. Cell Biol. 105:1987;1473.
6. Czop J.K., Austen F.K. A β-glucan inhibitable receptor on human monocytes: its identity with the phagocytic receptor for particulate activators of the alternative complement pathway. J. Immunol. 134:1985;2588.
7. Czop J.K., Kay J. Isolation and characterization of the β-glucan receptors on human mononuclear phagocytes. J. Exp. Med. 173:1991;1511.
8. Dilworth J.A., Hendley J.O., Mandell G.L. Attachment and ingestion of gonococci by human neutrophils. Infect. Immun. 11:1975;512.
9. Drevets D.A., Campbell P.A. Macrophage phagocytosis: use of fluorescence microscopy to distinguish between extracellular and intracellular bacteria. J. Immunol. Methods. 142:1991;31.
10. Ezekowitz R.A.B., Sim R.B., MacPherson G.G., Gordon S. Interaction of human monocytes, macrophages, and polymorphonuclear leukocytes with zymosan in vitro. Role of type 3 complement receptors and macrophage derived complement. J. Clin. Invest. 76:1985;2368.
11. Ezekowitz R.A.B., Satry K., Bailly P., Warner A. Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-I cells J. Exp. Med. 172:1990;1785.
12. Gerson D.F., Capo C., Benoliel A.M., Bongrand P. Adhesion, phagocytosis and cell surface energy. The binding of fixed human erythrocytes to rat macrophages and polymethylpentene. Biochim. Biophys. Acta. 692:1982;147.
13. Giaimis J., Lombard Y., Makaya-kumba M., Fonteneau P., Poindron P. A new and simple method for studying the binding and ingestion steps in the phagocytosis of yeast. J. Immunol. Methods. 154:1992;185.
14. Greenberg S., Silverstein S.C. Phagocytosis. Paul W.E. Fundamental Immunology. 1993;941 Raven Press, New York.
15. Greenberg S., Khoury J.E., Kaplan E., Silverstein S.C. A fluorescence technique to distinguish attached from ingested erythrocytes and zymosan particles in phagocytosing macrophages. J. Immunol. Methods. 139:1991;115.
16. Griffin F.M. Jr., Griffin J.A., Leider J.E., Silverstein S.C. Studies on the mechanism of phagocytosis. I. Requirements for circumferential attachment of particle-bound ligands to specific receptors on the macrophage plasma membrane. J. Exp. Med. 142:1975;1263.
17. Hed J. Methods for distinguishing ingested from adhering particles. Methods Enzymol. 132:1985;198.
18. Kruskal B.A., Sastry K., Warner A.B., Mathieu C.E., Ezekowitz R.A.B. Phagocytic chimeric receptors require both transmembrane and cytoplasmic domains from the mannose receptor. J. Exp. Med. 176:1992;1673.
19. Levitz S.M., DiBenedetto D.J., Diamond R.D. A rapid fluorescent assay to distinguish attached from phagocytized yeast particles. J. Immunol. Methods. 101:1987;37.
20. MacLean-Fletcher S., Pollard T.D. Mechanism of cytochalasin B on actin. Cell. 20:1980;329.
21. Mantovani B., Rabinovitch M., Nussenzweig V. Phagocytosis of immune complexes by macrophages. Different roles of the macrophage receptor sites for complement (C3) and for immunoglobulin (IgG). J. Exp. Med. 135:1972;780.
22. Mellman I., Fuchs R., Helenius A. Acidification of the endocytic and exocytic pathways. Annu. Rev. Biochem. 55:1986;663.
23. Ofek I., Sharon N. Lectinophagocytosis: a molecular mechanism of recognition between cell surface sugars and lectins in the phagocytosis of bacteria. Infect. Imunn. 56:1998;539.
24. Painter R.G., Whisenand J., McIntosh A.T. Effects of cytochalasin B on actin and myosin association with particle binding sites in mouse macrophages: implications with regard to the mechanism of action of the cytochalasins. J. Cell Biol. 91:1981;373.
25. Parod R.J., Brian J.D. Immune opsonin-independent phagocytosis by pulmonary macrophages. J. Immunol. 136:1986;2041.
26. Phaf H.J. Cell wall of yeasts. Annu. Rev. Microbiol. 17:1963;15.
27. Rabinovitch M. The dissociation of the attachment and ingestion phases of phagocytosis by macrophages. Exp. Cell Res. 46:1967;19.
28. Ross G.D., Cain J.A., Lachman P.J. Membrane complement receptor type three (CR3) has lectin-like properties analogous to bovine conglutinin and functions as a receptor for zymosan and rabbit erythrocytes as well as a receptor for zymosan and rabbit erythrocytes as well as receptor for iC3b. J. Immunol. 134:1985;3307.
29. Shaw D.R., Griffin F.M. Antibody-dependent and antibody-independent phagocytosis. Adams D.O., Edelson P.J., Koren H.S. Methods For Studying Mononuclear Phagocytes. 1981;511 Academic Press, San Diego, CA.
30. Silverstein S.C., Steinman R.M., Cohn Z.A. Endocytosis. Annu. Rev. Biochem. 46:1977;669.
31. Stahl P., Schlesinger P.H., Sigardson E., Rodman J.S., Lee Y.C. Receptor-mediated pinocytosis of mannose glycoconjugates by macrophages: characterization and evidence of receptor recycling. Cell. 19:1980;207.
32. Stephenson J.D., Shephered V.L. Purification of the human alveolar macrophage mannose receptor. Biochem. Biophys. Res. Commun. 148:1987;883.
33. Sung S.J., Nelson R.S., Silverstein S.C. Yeast mannans inhibit binding and phagocytosis of zymosan by mouse peritoneal macrophages. J. Cell Biol. 96:1983;160.
34. Sung S.J., Nelson R.S., Silverstein S.C. The role of the mannose/N-acetylglucosamine receptor in the pinocytosis of horseradish peroxidase by mouse peritoneal macrophages. J. Cell Physiol. 116:1983;21.
35. Thornton B.P., Vetvicka V., Pitman M., Goldman R.C., Ross G.D. Analysis of the sugar specificity and molecular localization of the β-glucan-binding lectin site of complement receptor type 3 (CD11b/CD 18). J. Immunol. 156:1996;1235.
36. Tietze C., Schlesinger P., Stahl P. Chloroquine and ammonium ion inhibit receptor-mediated endocytosis of mannose-glycoconjugates: apparent inhibition of receptor recycling. Biochem. Biophys. Res. Commun. 93:1980;1.
37. Tran Van Nhieu G., Isberg R.R. Bacterial internalization mediated by β1 chain integrins is determined by ligand affinity and receptor density. EMBO J. 12:1993;1887.
38. Verhoef J., Waldvogel F.A. Testing phagocytic cell function. Eur. J. Clin. Microbiol. 4:1985;379.
39. Vogel G., Thilo L., Schwarz H., Steinhart R. Mechanism of phagocytosis in Dictyostelium discoideum: phagocytosis is mediated by different recognition sites as disclosed by mutants with altered phagocytic properties. J. Cell Biol. 86:1980;456.
40. Wright S.D., Licht M.R., Graigmyle L.S., Silverstein S.C. Communication between receptors for different ligands on a single cell: ligation of fibronectin receptors induces a reversible alteration in the function of complement receptors on cultured human monocytes. J. Cell Biol. 99:1984;336.
41. Zigmond S.H., Hirsch J.G. Effects of cytochalasin B on polymorphonuclear leukocyte locomotion, phagocytosis, and glycolysis. Exp. Cell Res. 73:1972;383.